Sulfur Administration in Fe–S Cluster Homeostasis

Abstract

Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein synthesis or undergo further transformation. Mitochondrial Fe–S cluster biogenesis components are required in the cytosolic iron–sulfur cluster assembly machinery for cytosolic and nuclear cluster supplies. Clusters that are the key components of Fe–S proteins are vulnerable and prone to degradation whenever exposed to oxidative stress. However, once degraded, the Fe–S cluster can be resynthesized or repaired. It has been proposed that sulfurtransferases, rhodanese, and 3-mercaptopyruvate sulfurtransferase, responsible for sulfur transfer from donor to nucleophilic acceptor, are involved in the Fe–S cluster formation, maturation, or reconstitution. In the present paper, we attempt to sum up our knowledge on the involvement of sulfurtransferases not only in sulfur administration but also in the Fe–S cluster formation in mammals and yeasts, and on reconstitution-damaged cluster or restoration of enzyme’s attenuated activity.

Optimization of a Method for Detecting Intracellular Sulfane Sulfur Levels and Evaluation of Reagents That Affect the Levels in Escherichia coli

“…The acid-labile sulfur, including Fe-S clusters, is sulfide [ 52 , 53 ]. When O 2 •− and HO• oxidize Fe-S clusters and release Fe 2+ [ 54 , 55 , 56 ], the sulfur in the cluster is theoretically oxidized to sulfane sulfur (zero valences), as sulfide reacts with ROS to produce sulfane sulfur [ 57 ]. H 2 O 2 and tBH were unable to increase iSS ( Figure 7 A), perhaps partly because they are rapidly metabolized by E. coli cells [ 58 ], partly because they react with sulfane sulfur at a relatively slow rate [ 40 ], and partly because they do not directly damage Fe-S clusters [ 59 ].…”

Sulfurtransferases and Cystathionine Beta-Synthase Expression in Different Human Leukemia Cell Lines

“…Mitochondrial sulfurtransferases, TST and MPST, participate in the formation of iron-sulfur (Fe-S) clusters [ 23 ]. Both enzymes, which are highly expressed in AML (MOLM-14, MV4-11) as well as B-ALL (REH) cells, may therefore play an important role in the formation of Fe-S clusters that are components of the respiratory chain complexes.…”

“…Sulfurtransferases (thiosulfate sulfurtransferase, TST, rhodanese; 3-mercaptopyruvate sulfurtransferase, MPST; gamma-cystathionase, CTH) and cystathionine beta-synthase (CBS) are involved in l -cysteine metabolism [ 15 ]. These enzymes participate in: the formation of sulfane sulfur-containing compounds (TST, MPST, CTH) [ 16 ]; hydrogen sulfide (H 2 S) production (MPST, CTH, CBS) [ 17 , 18 , 19 ]; protection against oxidative stress (MPST, TST) [ 20 , 21 ]; mitochondrial bioenergetics (TST, MPST) [ 22 , 23 ]; glucose and lipid metabolism (MPST, TST) [ 24 , 25 ]; and cyanide detoxification (TST, MPST, CTH) [ 25 , 26 ]. Abe and Kimura [ 17 ] for the first time reported that H 2 S, which is produced in the brain largely by CBS, may also function as an endogenous neuromodulator.…”

Thiosulfate-Cyanide Sulfurtransferase a Mitochondrial Essential Enzyme: From Cell Metabolism to the Biotechnological Applications

“…All of these functions are summarized in the Figure 3 . The persulfide intermediate (ES form) of the enzyme acts as a sulfur-carrier and plays a critical role in sulfur trafficking by delivering sulfur in a “safe” chemical species in several biosynthetic pathways [ 65 , 66 , 67 ]. TST is able to interact with enzymes of oxidative metabolism, such as succinate dehydrogenase [ 64 ], NADH dehydrogenase [ 68 ], xanthine oxidase [ 69 ] and NADH nitrate reductase [ 8 ].…”